Structural Classification of Proteins
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Protein: Dihydrodipicolinate synthase from Mycobacterium tuberculosis [TaxId: 1773]

SQ P63945 5-300

Lineage:

  1. Root: scop
  2. Class: Alpha and beta proteins (a/b) [51349]
    Mainly parallel beta sheets (beta-alpha-beta units)
  3. Fold: TIM beta/alpha-barrel [51350]
    contains parallel beta-sheet barrel, closed; n=8, S=8; strand order 12345678
    the first seven superfamilies have similar phosphate-binding sites
  4. Superfamily: Aldolase [51569]
    Common fold covers whole protein structure
    link to SUPERFAMILY database - Superfamily
  5. Family: Class I aldolase [51570]
    the catalytic lysine forms schiff-base intermediate with substrate
    possible link between the aldolase superfamily and the phosphate-binding beta/alpha barrels
  6. Protein: Dihydrodipicolinate synthase [51574]
  7. Species: Mycobacterium tuberculosis [TaxId: 1773] [141831]
    SQ P63945 5-300

PDB Entry Domains:

  1. 1xxx picpic
    complexed with cl, dtt, mg
    1. region a:5-300 [122433] picpiclink
  2. 1xxx picpic
    automatically matched to 1XXX A:5-300
    complexed with cl, dtt, mg
    1. region b:6-300 [122434] picpiclink
  3. 1xxx picpic
    automatically matched to 1XXX A:5-300
    complexed with cl, dtt, mg
    1. region c:5-300 [122435] picpiclink
  4. 1xxx picpic
    automatically matched to 1XXX A:5-300
    complexed with cl, dtt, mg
    1. region d:6-300 [122436] picpiclink
  5. 1xxx picpic
    automatically matched to 1XXX A:5-300
    complexed with cl, dtt, mg
    1. region e:6-300 [122437] picpiclink
  6. 1xxx picpic
    automatically matched to 1XXX A:5-300
    complexed with cl, dtt, mg
    1. region f:5-300 [122438] picpiclink
  7. 1xxx picpic
    automatically matched to 1XXX A:5-300
    complexed with cl, dtt, mg
    1. region g:6-300 [122439] picpiclink
  8. 1xxx picpic
    automatically matched to 1XXX A:5-300
    complexed with cl, dtt, mg
    1. region h:5-300 [122440] picpiclink

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MRC
site Generated from scop database 1.75 with scopm 1.101 on Wed Jun 3 10:42:06 2009
Copyright © 1994-2009 The scop authors / scop@mrc-lmb.cam.ac.uk